TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei

Yeonchul Hong; Kisaburo Nagamune; Kazuhito Ohishi; Yasu S. Morita; Hisashi Ashida; Yusuke Maeda; Taroh Kinoshita

doi:10.1016/j.febslet.2005.12.075

TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei

Yeonchul Hong, Kisaburo Nagamune, Kazuhito Ohishi, Yasu S. Morita, Hisashi Ashida, Yusuke Maeda, Taroh Kinoshita

Department of Medicine

Osaka University

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

Abstract

Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.

Original language	English
Pages (from-to)	603-606
Number of pages	4
Journal	FEBS Letters
Volume	580
Issue number	2
DOIs	https://doi.org/10.1016/j.febslet.2005.12.075
State	Published - 23 Jan 2006

Keywords

Endoplasmic reticulum
Glycosylphosphatidylinositol
Intermolecular disulfide bond
Post-translational modification
Transamidase

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10.1016/j.febslet.2005.12.075

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title = "TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei",

abstract = "Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.",

keywords = "Endoplasmic reticulum, Glycosylphosphatidylinositol, Intermolecular disulfide bond, Post-translational modification, Transamidase",

author = "Yeonchul Hong and Kisaburo Nagamune and Kazuhito Ohishi and Morita, {Yasu S.} and Hisashi Ashida and Yusuke Maeda and Taroh Kinoshita",

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T1 - TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei

AU - Hong, Yeonchul

AU - Nagamune, Kisaburo

AU - Ohishi, Kazuhito

AU - Morita, Yasu S.

AU - Ashida, Hisashi

AU - Maeda, Yusuke

AU - Kinoshita, Taroh

PY - 2006/1/23

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N2 - Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.

AB - Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.

KW - Endoplasmic reticulum

KW - Glycosylphosphatidylinositol

KW - Intermolecular disulfide bond

KW - Post-translational modification

KW - Transamidase

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DO - 10.1016/j.febslet.2005.12.075

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JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei

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Keywords

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